The Isolation of an O-diphenal Oxidase from Third-instar Larvae of the Blowfly Calliphora Erythrocephala
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1. The isolation of an o-diphenol oxidase from an acetone-dried powder of late-third-instar larvae of Calliphora erythrocephala was investigated. An insoluble and micro-crystalline fraction containing the enzyme activity was obtained after fractionating extracts of the acetone-dried powder with (NH4)2SO4 and acetone. 2. This fraction can be solubilized in 0.1% sodium dodecyl sulphate without loss of activity. 3. Polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate shows that the o-diphenol oxidase is a minor component of the extracts from the acetone-dried powder. 4. The o-diphenol oxidase was purified by zonal centrifugation on a sucrose density gradient in the presence of sodium dodecyl sulphate. 5. The amino acid composition of the purified enzyme resembles that of some other o-diphenol oxidases. 6. The subunit composition of the o-diphenol oxidase is discussed.
A compilation of amino acid analyses of proteins : XVII. Residues per thousand residues-4.
Kirschenbaumt D Appl Biochem Biotechnol. 2013; 7(5):343-84.
PMID: 24234363 DOI: 10.1007/BF02798319.
Hall M, Scott T, Sugumaran M, Soderhall K, Law J Proc Natl Acad Sci U S A. 1995; 92(17):7764-8.
PMID: 7644492 PMC: 41226. DOI: 10.1073/pnas.92.17.7764.